calorimetry is a particularly advantageous method used to study the thermodynamics of binding interactions (e.g., protein-protein interactions, proteins-DNA, drug-protein interactions) of biological and/or pharmaceutical compounds. Calorimetry measures the energy released or absorbed by a reaction over a range of reactant concentrations, and uses this information to determine the thermodynamic properties, stoichiometry, and equilibrium binding constant for the reaction.
Temperature sensors conventionally employed for determining the heat of a chemical reaction in calorimetry studies include thermocouples, thermopiles, and/or thermistors. Other temperature sensing methods include sensors with microfluidic channels and have used changes in optical properties to infer temperature changes in reactions. However, these optical-based temperature-sensing approaches often lack a desired sensitivity for detecting small changes in temperature. In addition, the occurrence of air bubbles in microfluidic channels can have a deleterious effect on optical-based approaches.